2019-nCoV Spike protein RBD (K417N) (C19SD-G236H)

2019-nCoV Spike protein RBD (K417N) (C19SD-G236H)

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Description: Recombinant 2019-nCoV Spike protein S1 subunit, RBD (K417N) (319-541) was expressed in CHO cells using a C-terminal his tag.

Species: SARS-CoV-2

Tag: HIS tag

Expression System: CHO Cells

Sequence: 319-541

Genbank Number: MN908947

Purity: The purity of 2019-nCoV Spike protein RBD (K417N) was determined to be >90% by densitometry, approx. MW 39 kDa.



Activity: Binding ability measured in a functional ELISA. 2019-nCoV spike protein RBD (K417N) binds to immobilized human ACE2 (19-740) protein (A51C2-G341F).

Storage and Stability: Store product at –70oC. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.

Molecular Weight: 39 kDa

Gene Aliases : 2019-nCoV RBD, SARS-CoV-2 spike RBD, novel coronavirus spike RBD, nCov spike RBD.

Scientific Background: The receptor binding domain (RBD) of the SARS-CoV-2 spike glycoprotein recognizes the host ACE2 receptor and is a major determinant of viral entry and neutralization (1). K417N mutation in the RBD region of spike protein has been identified in B.1.351 lineages. In addition to antigenic effect, K417N alters binding affinity to ACE-2 protein. As new variants displace the first-wave virus, it is pivotal to evaluate their transmissibility, virulence and their possible tendency to escape antibody neutralization (2, 3).

References : 

1. Lan J, et al: Crystal structure of the 2019-nCov spike receptor-binding domain bound with the ACE2 receptor. bioRxiv. doi: https://doi.org/10.1101/2020.02.19.956235.

2. Harvey, WT, et al: SARS-CoV-2 variants, spike mutations and immune escape. Nat Rev Microbiol. 2021, 19:409–424.

3. Starr TN, et al: Deep mutational scanning of SARS-CoV-2 receptor binding domain reveals constraints on folding and ACE2 binding. Cell. 2020, 182(5):1295-1310.


Product Sheets (By Lot #) :

F3844-12